• ISSN 1008-505X
  • CN 11-3996/S
孙琳琳, 辛士超, 强晓晶, 程宪国. 非生物胁迫下植物水通道蛋白的应答与调控[J]. 植物营养与肥料学报, 2015, 21(4): 1040-1048. DOI: 10.11674/zwyf.2015.0424
引用本文: 孙琳琳, 辛士超, 强晓晶, 程宪国. 非生物胁迫下植物水通道蛋白的应答与调控[J]. 植物营养与肥料学报, 2015, 21(4): 1040-1048. DOI: 10.11674/zwyf.2015.0424
SUN Lin-lin, XIN Shi-chao, QIANG Xiao-jing, CHENG Xian-guo. Responsive regulation of aquaporins in the plants exposed to abiotic stresses[J]. Journal of Plant Nutrition and Fertilizers, 2015, 21(4): 1040-1048. DOI: 10.11674/zwyf.2015.0424
Citation: SUN Lin-lin, XIN Shi-chao, QIANG Xiao-jing, CHENG Xian-guo. Responsive regulation of aquaporins in the plants exposed to abiotic stresses[J]. Journal of Plant Nutrition and Fertilizers, 2015, 21(4): 1040-1048. DOI: 10.11674/zwyf.2015.0424

非生物胁迫下植物水通道蛋白的应答与调控

Responsive regulation of aquaporins in the plants exposed to abiotic stresses

  • 摘要: 【目的】水分不仅是细胞中各类生命物质合成的必需底物,而且也参与植物体内的养分代谢和渗透平衡的调节。植物中水分的跨膜转运主要是由水通道蛋白(AQPs)所介导的,因此,无论是在植物整体水平还是细胞水平上,水分的吸收以及跨细胞膜系统的转运对于植物的生长发育都是至关重要的。近年来,水通道蛋白作为调节水分的吸收与转运的关键,已成为植物营养与分子生物学特别关注和研究的热点之一。本文从水通道蛋白的种类结构,底物特异性,基因表达特征和调控机制四个方面对水通道蛋白转运水分的机理和转运水分过程中对胁迫的响应机制进行了详细阐述;从水通道蛋白的水分运输和渗透调节功能及其养分运输功能两方面说明了水通道蛋白在植物生长过程中的生理作用;阐述了光照、干旱和低温与水通道蛋白功能之间的关系,明确了水通道蛋白通过表达量的增加或者降低来响应相应环境条件的变化。【主要机理】 水通道蛋白通过保持一定结构及对底物运输的特异性来实现对水分的高效运输,通过调整基因的表达量和翻译后修饰等过程实现对水分的高效转运;同时,水通道蛋白可以通过水分的运输实现植物渗透平衡的调节,对部分小分子养分的吸收等功能更是实现了对植物生理和养分吸收的调节;另外,水通道蛋白不仅可以提高植物的抗旱、抗盐能力,对低温胁迫也有一定的响应,还可以与多类逆境胁迫蛋白发生相互作用,共同调节植物的水分和渗透平衡,提高植物应对逆境胁迫的能力,表明植物水通道蛋白对非生物胁迫下的应答机制有待于进一步探索,为植物水通道蛋白的应用研究提供科学的理论支持与材料支撑。

     

    Abstract: Water is not only a necessary substrate synthesizing living matter in organisms, but also involves in the nutrient metabolism and the osmotic adjustment in the plant. Transmembrane transport of water in plants is mainly carried out by the water channel protein (AQPs) mediation. Therefore, based the overall level of plants or cell level, the moisture absorption and transport across the membrane system are essential guarantee for plant growth and development. In recent years, aquaporin, as a key factor regulating the water absorption and translation, has been widely focused in the research fields of plant nutrition and stress physiology at molecular level. This review described the mechanism of water transport involved by AQPs and the responsemechanism of the AQPs to abiotic stresses based on the kinds of structure, substrate specificity, gene expression and regulation mechanism of aquaporin in plants, and the physiological effects of water channel protein during plant growth process were better described, and functionally characterized the transport mechanism of water and osmotic adjustment as well as nutrient transport models regulated by channel protein. The responses of aquaporin proteins to the changes of environment factors such as the strength of light, drought and low temperature, were discussed accordingly. Study showed that the water channel protein obviously responded to the environmental changes by increasing or reducing the accumulation amounts of AQS expression, and aquaporin could realize an efficient transport of water in plants by maintaining certain specific structures and the transport of substrate specificity as well as adjusting the expression of target genes and post-translational modification processes. Importantly, aquaporin plays a positive role in maintianing an equilibrium of osmotic potentials by transport regulation of water and absorption of small molecule chemicals, which are involved in the physiological regulation and nutrient uptake in the plants. Aquaporin can not only enhance the tolerance of plant to drought and salt stress, but also to cold stress. Moreover, aquaporin could interact with proteins that responds to abiotic stresses, and regulate osmotic equilibrium in the plant cells to improve the adaptation ability of plant exposed to abiotic stresses. Responsive mechanism of water channel protein in the plants exposing to abiotic stresses should be further investigated in the coming exploration to provide scientific supports and molecular materials for application of aquaporin in molecular breeding.

     

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